(data stored in ACNUC6288 zone)

SWISSPROT: EIF3B_DEBHA

ID   EIF3B_DEBHA             Reviewed;         719 AA.
AC   Q6BLY5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 107.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3 p90 {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Translation initiation factor eIF3 p90 subunit homolog;
GN   Name=PRT1 {ECO:0000255|HAMAP-Rule:MF_03001};
GN   OrderedLocusNames=DEHA2F09768g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with
CC       other initiation factors, stimulates binding of mRNA and
CC       methionyl-tRNAi to the 40S ribosome. The eIF-3 complex
CC       specifically targets and initiates translation of a subset of
CC       mRNAs involved in cell proliferation. {ECO:0000255|HAMAP-
CC       Rule:MF_03001}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC       3 (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family.
CC       {ECO:0000255|HAMAP-Rule:MF_03001}.
DR   EMBL; CR382138; CAG89127.2; -; Genomic_DNA.
DR   RefSeq; XP_460786.2; XM_460786.1.
DR   STRING; 4959.XP_460786.2; -.
DR   EnsemblFungi; CAG89127; CAG89127; DEHA2F09768g.
DR   GeneID; 2904198; -.
DR   KEGG; dha:DEHA2F09768g; -.
DR   HOGENOM; HOG000265546; -.
DR   InParanoid; Q6BLY5; -.
DR   KO; K03253; -.
DR   OMA; DAKLHWQ; -.
DR   OrthoDB; 1194797at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR   GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011400; EIF3B.
DR   InterPro; IPR034363; eIF3B_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   PANTHER; PTHR14068; PTHR14068; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BLY5.
DR   SWISS-2DPAGE; Q6BLY5.
KW   Coiled coil; Complete proteome; Cytoplasm; Initiation factor;
KW   Protein biosynthesis; Reference proteome; Repeat; RNA-binding;
KW   WD repeat.
FT   CHAIN         1    719       Eukaryotic translation initiation factor
FT                                3 subunit B.
FT                                /FTId=PRO_0000363818.
FT   DOMAIN       41    128       RRM. {ECO:0000255|HAMAP-Rule:MF_03001}.
FT   REPEAT      194    233       WD 1.
FT   REPEAT      234    295       WD 2.
FT   REPEAT      305    343       WD 3.
FT   REPEAT      346    388       WD 4.
FT   REPEAT      456    501       WD 5.
FT   REPEAT      517    559       WD 6.
FT   REPEAT      573    618       WD 7.
FT   REGION        1    228       Sufficient for interaction with PIC8.
FT                                {ECO:0000255|HAMAP-Rule:MF_03001}.
FT   REGION        1    102       Sufficient for interaction with HCR1 and
FT                                TIF32. {ECO:0000255|HAMAP-Rule:MF_03001}.
SQ   SEQUENCE   719 AA;  82134 MW;  78BA6E17AAA9D88F CRC64;
     MNDNMSEQEY RSLEKEVQLD DLDFSDLEAK YAVNSDFGMD NYVVVDGAPI APEAKVPILI
     KVLKKLFNTV GEVVEGDEGI HMPLQDGKSK GYLFVQFKTP QMAEAAIQQL HGKKLDQKHR
     LLVNKLSDIE KFGAEGNVEI DFHEPEIPPF KSHGYLRSWL QDEQGRDQMA LHFSETVGVY
     YNKKKNDPEP VIEPRKGFTS KYAKFSPLGT YLFSVHPQGV QSWGGDGFQS ITKFIHNQVR
     LIDFSPNEKY MVTLSPLPIA LPDDPAERSI FPFGPESNGH KLVIWDMATG EPARTFALPP
     HLEGQKDMPW PLVKWSHDDK YCARQGPGAL AIYETPSFQL LDKKLVKVDD VVDFEWAPAA
     VHLSDSKVKE GEYILSYWTP ESSNQTARVA LMQIPSRKVI RTINLFQVSD CKMHWHGEGK
     FLCVKVDRHT KSRKTFFSNL EFFKVTEKDI PVEKLELKDV VFNFAWEPRS ERFITISRLD
     DGNQNPSIAK NTISFYAPQV SSKGRVTSSK YTCFKEIHDK HSNTVCWSPK GRFVVVATIS
     KSSGELEFYD CSYEEDKPAN SKVNGNVKLL KAEKYSGMTN LAWDPSGRFV AAWSSSWAHS
     IENGYRLFEF TGNMLKDNSI DHFKEFIWRP RPASLLNAAD RKKVRKNLRE YSAQFDEADA
     MEADAASREA ILLRRKLLEQ WRSYRAKHAA NGSKKNEVQA EIIEEIKEEI IEEKEEVVE
//

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